ID Q65MX0_BACLD Unreviewed; 512 AA.
AC Q65MX0; Q62YB3;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE SubName: Full=Alpha amylase, Glycoside Hydrolase Family 13 {ECO:0000313|EMBL:AAU22245.1};
GN Name=amyL {ECO:0000313|EMBL:AAU22245.1};
GN OrderedLocusNames=BL00499 {ECO:0000313|EMBL:AAU22245.1};
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU22245.1, ECO:0000313|Proteomes:UP000000606};
RN [1] {ECO:0000313|EMBL:AAU22245.1, ECO:0000313|Proteomes:UP000000606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC {ECO:0000313|Proteomes:UP000000606};
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; CP000002; AAU22245.1; -; Genomic_DNA.
DR RefSeq; WP_011197602.1; NC_006322.1.
DR AlphaFoldDB; Q65MX0; -.
DR SMR; Q65MX0; -.
DR STRING; 279010.BL00499; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 66217199; -.
DR KEGG; bli:BL00499; -.
DR PATRIC; fig|279010.13.peg.639; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_024572_2_0_9; -.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11318; AmyAc_bac_fung_AmyA; 1.
DR Gene3D; 2.40.30.140; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013776; A-amylase_thermo.
DR InterPro; IPR015237; Alpha-amylase_C_pro.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF09154; Alpha-amy_C_pro; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW Hydrolase {ECO:0000313|EMBL:AAU22245.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000606};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..512
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004268998"
FT DOMAIN 34..420
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 260
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT ACT_SITE 290
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 436
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ SEQUENCE 512 AA; 58529 MW; E3F8F560C3419D9D CRC64;
MKQQKRLYAR LLPLLFALIF LLPHSAAAAA NLKGTLMQYF EWYMPNDGQH WKRLQNDSAY
LAEHGITAVW IPPAYKGTSQ ADVGYGAYDL YDLGEFHQKG TVRTKYGTKG ELQSAIKSLH
SRDINVYGDV VINHKGGADA TEDVTAVEVD PADRNRVISG EHRIKAWTHF HFPGRGSTYS
DFKWHWYHFD GTDWDESRKL NRIYKFQGKA WDWEVSNENG NYDYLMYADI DYDHPDVAAE
IKRWGTWYAN ELQLDGFRLD AVKHIKFSFL RDWVNHVREK TGKEMFTVAE YWQNDLGALE
NYLNKTNFNH SVFDVPLHYQ FHAASTQGGG YDMRKLLNGT VVSKHPLKAV TFVDNHDTQP
GQSLESTVQT WFKPLAYAFI LTRESGYPQV FYGDMYGTKG DSQREIPALK HKIEPILKAR
KQYAYGAQHD YFDHHDIVGW TREGDSSVAN SGLAALITDG PGGAKRMYVG RQNAGETWHD
ITGNRSEPVV INSEGWGEFH VNGGSVSIYV QR
//
